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Database: UniProt
Entry: S8D5W5_9LAMI
LinkDB: S8D5W5_9LAMI
Original site: S8D5W5_9LAMI 
ID   S8D5W5_9LAMI            Unreviewed;       404 AA.
AC   S8D5W5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=cytokinin dehydrogenase {ECO:0000256|ARBA:ARBA00011928};
DE            EC=1.5.99.12 {ECO:0000256|ARBA:ARBA00011928};
DE   Flags: Fragment;
GN   ORFNames=M569_16809 {ECO:0000313|EMBL:EPS58008.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS58008.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS58008.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal +
CC         adenine + AH2; Xref=Rhea:RHEA:13625, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15825, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:17660; EC=1.5.99.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001689};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS58008.1}.
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DR   EMBL; AUSU01009628; EPS58008.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8D5W5; -.
DR   OrthoDB; 455805at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0019139; F:cytokinin dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016170; Cytok_DH_C_sf.
DR   InterPro; IPR015345; Cytokinin_DH_FAD/cytokin-bd.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878:SF112; CYTOKININ DEHYDROGENASE 7; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF09265; Cytokin-bind; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT   DOMAIN          48..222
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS58008.1"
SQ   SEQUENCE   404 AA;  44028 MW;  7FCBE71DD427B85B CRC64;
     IERFVKETDV DAVPEKGSAA EDSSLFCGVE VEFAGCGSHA GADFGGLQYT KPLAVVRPST
     ADDVAKIVRM AGRSPSLTVA ARGNGHSVNG QAMAHRGLVL DMKSLEIGID VYPEILQADV
     SGGALWEDVL KRCVSGFRLA PRSWTDYLGL TVGGTLSNAG VSGQTFLHGP QTENVTELEV
     VTGNGDVLVC SDHQNSDLFY AALGGLGQFG IITRARILLQ PVPDKVRWIR VVYSEFGDFT
     GDAESVVARP PQDNFDYLEG FVFVNGADPV NGWPSVPHRG QYFDPTRIPK SSGPVLYCLE
     LALHYDDEVP RSAIDKKVDR LIGGLRFVDG LRFEIDVGYA EFLTRVKRVE EDAKSNGIWE
     APHPWLNIFI SSEDVSEFDR LVFKKILRQG VGGPILVYPL LRSK
//
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